ID A0A0F7JQU8_9DEIO Unreviewed; 692 AA.
AC A0A0F7JQU8;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Serine protease {ECO:0000313|EMBL:AKH18122.1};
GN ORFNames=SY84_15095 {ECO:0000313|EMBL:AKH18122.1};
OS Deinococcus soli (ex Cha et al. 2016).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=1309411 {ECO:0000313|EMBL:AKH18122.1, ECO:0000313|Proteomes:UP000034024};
RN [1] {ECO:0000313|EMBL:AKH18122.1, ECO:0000313|Proteomes:UP000034024}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N5 {ECO:0000313|EMBL:AKH18122.1,
RC ECO:0000313|Proteomes:UP000034024};
RA Kim M.K., Srinivasan S., Lee J.-J.;
RT "Deinococcus soli/N5/whole genome sequencing.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase S8 family.
CC {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC ECO:0000256|RuleBase:RU003355}.
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DR EMBL; CP011389; AKH18122.1; -; Genomic_DNA.
DR RefSeq; WP_046844689.1; NZ_CP011389.1.
DR AlphaFoldDB; A0A0F7JQU8; -.
DR KEGG; dch:SY84_15095; -.
DR PATRIC; fig|1309411.5.peg.3081; -.
DR OrthoDB; 9790784at2; -.
DR Proteomes; UP000034024; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 1.
DR InterPro; IPR000209; Peptidase_S8/S53_dom.
DR InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR InterPro; IPR022398; Peptidase_S8_His-AS.
DR InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR Pfam; PF00082; Peptidase_S8; 1.
DR PRINTS; PR00723; SUBTILISIN.
DR SUPFAM; SSF52743; Subtilisin-like; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
DR PROSITE; PS51892; SUBTILASE; 1.
DR PROSITE; PS00136; SUBTILASE_ASP; 1.
DR PROSITE; PS00137; SUBTILASE_HIS; 1.
DR PROSITE; PS00138; SUBTILASE_SER; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW ProRule:PRU01240};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000034024};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW ProRule:PRU01240}.
FT DOMAIN 281..601
FT /note="Peptidase S8/S53"
FT /evidence="ECO:0000259|Pfam:PF00082"
FT REGION 317..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 289
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 342
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT ACT_SITE 553
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ SEQUENCE 692 AA; 70032 MW; EC3999DC0390ABF9 CRC64;
MTHLFGKAGL LVAALALTAC DQLHTAGVGV QDRTVALGLR AQQDVTVPFS GSWRIVEYPS
WVRVSKPAGT GAVALSVAAV RQDATPVAAD QAQLSGVIRV AWTTGSGADA KNGTAKWVVT
AQQYELTGRL SAPAAVTGTD VVTSVTGPQV GTPQARGVIV KYRSGLSAQS AQGAAGPLRA
DVRGRERLRA AGVSVQRHTP LGERSAALDV ADVKGALAAL RADPDVEYAV PNAVLRTQAM
NTQALATPVT PTDQFAPLQW AYPLLGYGAV WRDMEGGAYS RAVTVAVIDT GVRFDHPDLA
GALWGPGEGA LDVITDAANG DGTGPDTDPT DPSVPGRTTG SHGTHVTGII AARWGENSGV
CAGCSPSGVV GAAYKANVKV LPIRVIDAGG NATEADVTQG IRYAAGLPVT LDGVTYRSPH
PAQVINLSLG GAISAADAQP MCDAIAEARA AGSLVVAAAG NGYGTVPYYP AACDGAVAVG
SVTLSGASAP MHSAFSNAYP QVQLAAPGGA DPGSGATFNG GTFNTAPFPD MILSTGWNYV
KDAPNYEAEV GTSQASPQVA ALAALLLSKG VTTGPEDTLA RLRGTATDLG AAGRDDRFGF
GMINAAAALN APQVSSGLGV RVQSSRGLSF QPALDSTGAF RAFLGEGTYQ VVAGSDVNGN
GVYGESGETR DERAVTLSEA APRVTLGDLT PR
//
